메뉴 건너뛰기




Volumn 33, Issue 2, 2008, Pages 51-57

A permissive geometry model for TCR-CD3 activation

Author keywords

[No Author keywords available]

Indexed keywords

CD3 ANTIGEN; CD4 ANTIGEN; CD8 ANTIGEN; LYMPHOCYTE ANTIGEN RECEPTOR; PROTEIN SUBUNIT; T LYMPHOCYTE RECEPTOR;

EID: 38949089676     PISSN: 09680004     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tibs.2007.10.008     Document Type: Article
Times cited : (36)

References (54)
  • 1
    • 33748183257 scopus 로고    scopus 로고
    • The HAMP domain structure implies helix rotation in transmembrane signaling
    • Hulko M., et al. The HAMP domain structure implies helix rotation in transmembrane signaling. Cell 126 (2006) 929-940
    • (2006) Cell , vol.126 , pp. 929-940
    • Hulko, M.1
  • 2
    • 18744378545 scopus 로고    scopus 로고
    • A putative molecular-activation switch in the transmembrane domain of erbB2
    • Fleishman S.J., et al. A putative molecular-activation switch in the transmembrane domain of erbB2. Proc. Natl. Acad. Sci. U. S. A. 99 (2002) 15937-15940
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 15937-15940
    • Fleishman, S.J.1
  • 3
    • 0033543590 scopus 로고    scopus 로고
    • A piston model for transmembrane signaling of the aspartate receptor
    • Ottemann K.M., et al. A piston model for transmembrane signaling of the aspartate receptor. Science 1999 (1999) 1751-1754
    • (1999) Science , vol.1999 , pp. 1751-1754
    • Ottemann, K.M.1
  • 4
    • 0033548048 scopus 로고    scopus 로고
    • Erythropoietin receptor activation by a ligand-induced conformation change
    • Remy I., et al. Erythropoietin receptor activation by a ligand-induced conformation change. Science 283 (1999) 990-993
    • (1999) Science , vol.283 , pp. 990-993
    • Remy, I.1
  • 5
    • 33745223518 scopus 로고    scopus 로고
    • T-cell antigen-receptor stoichiometry: pre-clustering for sensitivity
    • Alarcon B., et al. T-cell antigen-receptor stoichiometry: pre-clustering for sensitivity. EMBO Rep. 7 (2006) 490-495
    • (2006) EMBO Rep. , vol.7 , pp. 490-495
    • Alarcon, B.1
  • 6
    • 0024980981 scopus 로고
    • Antigen receptor tail clue
    • Reth M. Antigen receptor tail clue. Nature 338 (1989) 383-384
    • (1989) Nature , vol.338 , pp. 383-384
    • Reth, M.1
  • 7
    • 33646181088 scopus 로고    scopus 로고
    • How TCRs bind MHCs, peptides, and coreceptors
    • Rudolph M.G., et al. How TCRs bind MHCs, peptides, and coreceptors. Annu. Rev. Immunol. 24 (2006) 419-466
    • (2006) Annu. Rev. Immunol. , vol.24 , pp. 419-466
    • Rudolph, M.G.1
  • 8
    • 0035967867 scopus 로고    scopus 로고
    • Mechanisms contributing to T cell receptor signaling and assembly revealed by the solution structure of an ectodomain fragment of the CD3εγ heterodimer
    • Sun Z.Y.J., et al. Mechanisms contributing to T cell receptor signaling and assembly revealed by the solution structure of an ectodomain fragment of the CD3εγ heterodimer. Cell 105 (2001) 913-923
    • (2001) Cell , vol.105 , pp. 913-923
    • Sun, Z.Y.J.1
  • 9
    • 9244252501 scopus 로고    scopus 로고
    • Crystal structure of a human CD3-epsilon/delta dimer in complex with a UCHT1 single-chain antibody fragment
    • Arnett K.L., et al. Crystal structure of a human CD3-epsilon/delta dimer in complex with a UCHT1 single-chain antibody fragment. Proc. Natl. Acad. Sci. U. S. A. 101 (2004) 16268-16273
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 16268-16273
    • Arnett, K.L.1
  • 10
    • 33750022623 scopus 로고    scopus 로고
    • The structure of the zetazeta transmembrane dimer reveals features essential for its assembly with the T cell receptor
    • Call M.E., et al. The structure of the zetazeta transmembrane dimer reveals features essential for its assembly with the T cell receptor. Cell 127 (2006) 355-368
    • (2006) Cell , vol.127 , pp. 355-368
    • Call, M.E.1
  • 11
    • 1242307780 scopus 로고    scopus 로고
    • Homooligomerization of the cytoplasmic domain of the T cell receptor zeta chain and of other proteins containing the immunoreceptor tyrosine-based activation motif
    • Sigalov A., et al. Homooligomerization of the cytoplasmic domain of the T cell receptor zeta chain and of other proteins containing the immunoreceptor tyrosine-based activation motif. Biochemistry 43 (2004) 2049-2061
    • (2004) Biochemistry , vol.43 , pp. 2049-2061
    • Sigalov, A.1
  • 12
    • 0037184955 scopus 로고    scopus 로고
    • The organizing principle in the formation of the T cell receptor-CD3 complex
    • Call M.E., et al. The organizing principle in the formation of the T cell receptor-CD3 complex. Cell 111 (2002) 967-979
    • (2002) Cell , vol.111 , pp. 967-979
    • Call, M.E.1
  • 13
    • 0037245720 scopus 로고    scopus 로고
    • Electrostatic fasteners hold the T cell receptor-CD3 complex together
    • Engelman D.M. Electrostatic fasteners hold the T cell receptor-CD3 complex together. Mol. Cell 11 (2003) 5-6
    • (2003) Mol. Cell , vol.11 , pp. 5-6
    • Engelman, D.M.1
  • 14
    • 33646718143 scopus 로고    scopus 로고
    • The assembly of diverse immune receptors is focused on a polar membrane-embedded interaction site
    • Feng J., et al. The assembly of diverse immune receptors is focused on a polar membrane-embedded interaction site. PLoS Biol. 4 (2006) e142
    • (2006) PLoS Biol. , vol.4
    • Feng, J.1
  • 15
    • 33947173844 scopus 로고    scopus 로고
    • Disruption of extracellular interactions impairs T cell receptor-CD3 complex stability and signaling
    • Kuhns M.S., and Davis M.M. Disruption of extracellular interactions impairs T cell receptor-CD3 complex stability and signaling. Immunity 26 (2007) 357-369
    • (2007) Immunity , vol.26 , pp. 357-369
    • Kuhns, M.S.1    Davis, M.M.2
  • 16
    • 10044292911 scopus 로고    scopus 로고
    • Solution structure of the CD3epsilondelta ectodomain and comparison with CD3epsilongamma as a basis for modeling T cell receptor topology and signaling
    • Sun Z.Y., et al. Solution structure of the CD3epsilondelta ectodomain and comparison with CD3epsilongamma as a basis for modeling T cell receptor topology and signaling. Proc. Natl. Acad. Sci. U. S. A. 101 (2004) 16867-16872
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 16867-16872
    • Sun, Z.Y.1
  • 17
    • 0034948337 scopus 로고    scopus 로고
    • The TCR triggering puzzle
    • van der Merwe P.A. The TCR triggering puzzle. Immunity 14 (2001) 665-668
    • (2001) Immunity , vol.14 , pp. 665-668
    • van der Merwe, P.A.1
  • 18
    • 0019435154 scopus 로고
    • Does OKT3 monoclonal antibody react with an antigen-recognition structure on human T cells?
    • Chang T.W., et al. Does OKT3 monoclonal antibody react with an antigen-recognition structure on human T cells?. Proc. Natl. Acad. Sci. U. S. A. 78 (1981) 1805-1808
    • (1981) Proc. Natl. Acad. Sci. U. S. A. , vol.78 , pp. 1805-1808
    • Chang, T.W.1
  • 19
    • 0021264238 scopus 로고
    • The Fab fragment of a directly activating monoclonal antibody that precipitates a disulfide-linked heterodimer from a helper T cell clone blocks activation by either allogeneic Ia or antigen and self-Ia
    • Kaye J., and Janeway Jr. C.A. The Fab fragment of a directly activating monoclonal antibody that precipitates a disulfide-linked heterodimer from a helper T cell clone blocks activation by either allogeneic Ia or antigen and self-Ia. J. Exp. Med. 159 (1984) 1397-1412
    • (1984) J. Exp. Med. , vol.159 , pp. 1397-1412
    • Kaye, J.1    Janeway Jr., C.A.2
  • 20
    • 33746114879 scopus 로고    scopus 로고
    • The kinetic-segregation model: TCR triggering and beyond
    • Davis S.J., and van der Merwe P.A. The kinetic-segregation model: TCR triggering and beyond. Nat. Immunol. 7 (2006) 803-809
    • (2006) Nat. Immunol. , vol.7 , pp. 803-809
    • Davis, S.J.1    van der Merwe, P.A.2
  • 21
    • 0032192469 scopus 로고    scopus 로고
    • Initiation of signal transduction through the T cell receptor requires the peptide multivalent engagement of MHC ligands
    • Boniface J.J., et al. Initiation of signal transduction through the T cell receptor requires the peptide multivalent engagement of MHC ligands. Immunity 9 (1998) 459-466
    • (1998) Immunity , vol.9 , pp. 459-466
    • Boniface, J.J.1
  • 22
    • 0033710093 scopus 로고    scopus 로고
    • The relationship of MHC-peptide binding and T cell activation probed using chemically defined MHC class II oligomers
    • Cochran J.R., et al. The relationship of MHC-peptide binding and T cell activation probed using chemically defined MHC class II oligomers. Immunity 12 (2000) 241-250
    • (2000) Immunity , vol.12 , pp. 241-250
    • Cochran, J.R.1
  • 23
    • 21244497887 scopus 로고    scopus 로고
    • CD8+ cytotoxic T lymphocyte activation by soluble major histocompatibility complex-peptide dimers
    • Cebecauer M., et al. CD8+ cytotoxic T lymphocyte activation by soluble major histocompatibility complex-peptide dimers. J. Biol. Chem. 280 (2005) 23820-23828
    • (2005) J. Biol. Chem. , vol.280 , pp. 23820-23828
    • Cebecauer, M.1
  • 24
    • 31144479383 scopus 로고    scopus 로고
    • CD8 T Cells, like CD4 T Cells, are triggered by multivalent engagement of TCRs by MHC-peptide ligands but not by monovalent engagement
    • Stone J.D., and Stern L.J. CD8 T Cells, like CD4 T Cells, are triggered by multivalent engagement of TCRs by MHC-peptide ligands but not by monovalent engagement. J. Immunol. 176 (2006) 1498-1505
    • (2006) J. Immunol. , vol.176 , pp. 1498-1505
    • Stone, J.D.1    Stern, L.J.2
  • 25
    • 0032192470 scopus 로고    scopus 로고
    • CD8 expression allows T cell signaling by monomeric peptide-MHC complexes
    • Delon J., et al. CD8 expression allows T cell signaling by monomeric peptide-MHC complexes. Immunity 9 (1998) 467-473
    • (1998) Immunity , vol.9 , pp. 467-473
    • Delon, J.1
  • 26
    • 0038035145 scopus 로고    scopus 로고
    • The beta1 and beta3 integrins promote T cell receptor-mediated cytotoxic T lymphocyte activation
    • Doucey M.A., et al. The beta1 and beta3 integrins promote T cell receptor-mediated cytotoxic T lymphocyte activation. J. Biol. Chem. 278 (2003) 26983-26991
    • (2003) J. Biol. Chem. , vol.278 , pp. 26983-26991
    • Doucey, M.A.1
  • 27
    • 0038025412 scopus 로고    scopus 로고
    • T cell adhesion lowers the threshold for antigen detection
    • Randriamampita C., et al. T cell adhesion lowers the threshold for antigen detection. Eur. J. Immunol. 33 (2003) 1215-1223
    • (2003) Eur. J. Immunol. , vol.33 , pp. 1215-1223
    • Randriamampita, C.1
  • 28
    • 0033573822 scopus 로고    scopus 로고
    • Multivalent structure of an alphabetaT cell receptor
    • Fernandez-Miguel G., et al. Multivalent structure of an alphabetaT cell receptor. Proc. Natl. Acad. Sci. U. S. A. 96 (1999) 1547-1552
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 1547-1552
    • Fernandez-Miguel, G.1
  • 29
    • 33645892299 scopus 로고    scopus 로고
    • A conformation- and avidity-based proofreading mechanism for the TCR-CD3 complex
    • Schamel W.W., et al. A conformation- and avidity-based proofreading mechanism for the TCR-CD3 complex. Trends Immunol. 27 (2006) 176-182
    • (2006) Trends Immunol. , vol.27 , pp. 176-182
    • Schamel, W.W.1
  • 30
    • 23944469458 scopus 로고    scopus 로고
    • Coexistence of multivalent and monovalent TCRs explains high sensitivity and wide range of response
    • Schamel W.W., et al. Coexistence of multivalent and monovalent TCRs explains high sensitivity and wide range of response. J. Exp. Med. 202 (2005) 493-503
    • (2005) J. Exp. Med. , vol.202 , pp. 493-503
    • Schamel, W.W.1
  • 31
    • 14244261004 scopus 로고    scopus 로고
    • Twisting tails exposed: the evidence for TCR conformational change
    • Levin S.E., and Weiss A. Twisting tails exposed: the evidence for TCR conformational change. J. Exp. Med. 201 (2005) 489-492
    • (2005) J. Exp. Med. , vol.201 , pp. 489-492
    • Levin, S.E.1    Weiss, A.2
  • 32
    • 2042538051 scopus 로고    scopus 로고
    • Receptor clustering and transmembrane signaling in T cells
    • Cochran J.R., et al. Receptor clustering and transmembrane signaling in T cells. Trends Biochem. Sci. 26 (2001) 304-310
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 304-310
    • Cochran, J.R.1
  • 33
    • 0034914677 scopus 로고    scopus 로고
    • Oligomeric antigen receptors: a new view on signaling for the selection of lymphocytes
    • Reth M. Oligomeric antigen receptors: a new view on signaling for the selection of lymphocytes. Trend. Immunol. 22 (2001) 356-360
    • (2001) Trend. Immunol. , vol.22 , pp. 356-360
    • Reth, M.1
  • 34
    • 0037188899 scopus 로고    scopus 로고
    • Recruitment of Nck by CD3 epsilon reveals a ligand-induced conformational change essential for T cell receptor signaling and synapse formation
    • Gil D., et al. Recruitment of Nck by CD3 epsilon reveals a ligand-induced conformational change essential for T cell receptor signaling and synapse formation. Cell 109 (2002) 901-912
    • (2002) Cell , vol.109 , pp. 901-912
    • Gil, D.1
  • 35
    • 33846224785 scopus 로고    scopus 로고
    • Full activation of the T cell receptor requires both clustering and conformational changes at CD3
    • Minguet S., et al. Full activation of the T cell receptor requires both clustering and conformational changes at CD3. Immunity 26 (2007) 43-54
    • (2007) Immunity , vol.26 , pp. 43-54
    • Minguet, S.1
  • 36
    • 15044358353 scopus 로고    scopus 로고
    • Agonist/endogenous peptide-MHC heterodimers drive T cell activation and sensitivity
    • Krogsgaard M., et al. Agonist/endogenous peptide-MHC heterodimers drive T cell activation and sensitivity. Nature 434 (2005) 238-243
    • (2005) Nature , vol.434 , pp. 238-243
    • Krogsgaard, M.1
  • 37
    • 0033762433 scopus 로고    scopus 로고
    • Phosphorylation of T cell receptor zeta is regulated by a lipid dependent folding transition
    • Aivazian D., and Stern L.J. Phosphorylation of T cell receptor zeta is regulated by a lipid dependent folding transition. Nat. Struct. Biol. 7 (2000) 1023-1026
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 1023-1026
    • Aivazian, D.1    Stern, L.J.2
  • 38
    • 34447278825 scopus 로고    scopus 로고
    • TCR recognition of peptide/MHC class II complexes and superantigens
    • Sundberg E.J., et al. TCR recognition of peptide/MHC class II complexes and superantigens. Semin. Immunol. 19 (2007) 262-271
    • (2007) Semin. Immunol. , vol.19 , pp. 262-271
    • Sundberg, E.J.1
  • 39
    • 0026550901 scopus 로고
    • Tetrameric cell-surface MHC class I molecules
    • Krishna S., et al. Tetrameric cell-surface MHC class I molecules. Nature 357 (1992) 164-167
    • (1992) Nature , vol.357 , pp. 164-167
    • Krishna, S.1
  • 40
    • 0028181870 scopus 로고
    • Clustering of class I HLA molecules on the surfaces of activated and transformed human cells
    • Matko J., et al. Clustering of class I HLA molecules on the surfaces of activated and transformed human cells. J. Immunol. 152 (1994) 3353-3360
    • (1994) J. Immunol. , vol.152 , pp. 3353-3360
    • Matko, J.1
  • 41
    • 12644304905 scopus 로고    scopus 로고
    • HLA class I and II antigens are partially co-clustered in the plasma membrane of human lymphoblastoid cells
    • Jenei A., et al. HLA class I and II antigens are partially co-clustered in the plasma membrane of human lymphoblastoid cells. Proc. Natl. Acad. Sci. U. S. A. 94 (1997) 7269-7274
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 7269-7274
    • Jenei, A.1
  • 42
    • 2142639533 scopus 로고    scopus 로고
    • Determination of structural principles underlying three different modes of lymphocytic choriomeningitis virus escape from CTL recognition
    • Velloso L.M., et al. Determination of structural principles underlying three different modes of lymphocytic choriomeningitis virus escape from CTL recognition. J. Immunol. 172 (2004) 5504-5511
    • (2004) J. Immunol. , vol.172 , pp. 5504-5511
    • Velloso, L.M.1
  • 43
    • 0029440613 scopus 로고
    • The structure of MHC class II: a role for dimer of dimers
    • Schafer P.H., et al. The structure of MHC class II: a role for dimer of dimers. Semin. Immunol. 7 (1995) 389-398
    • (1995) Semin. Immunol. , vol.7 , pp. 389-398
    • Schafer, P.H.1
  • 44
    • 0035871630 scopus 로고    scopus 로고
    • Clustering of class I HLA oligomers with CD8 and TCR: three-dimensional models based on fluorescence resonance energy transfer and crystallographic data
    • Gaspar Jr. R., et al. Clustering of class I HLA oligomers with CD8 and TCR: three-dimensional models based on fluorescence resonance energy transfer and crystallographic data. J. Immunol. 166 (2001) 5078-5086
    • (2001) J. Immunol. , vol.166 , pp. 5078-5086
    • Gaspar Jr., R.1
  • 45
    • 0142219443 scopus 로고    scopus 로고
    • A correlation between TCR Valpha docking on MHC and CD8 dependence: implications for T cell selection
    • Buslepp J., et al. A correlation between TCR Valpha docking on MHC and CD8 dependence: implications for T cell selection. Immunity 19 (2003) 595-606
    • (2003) Immunity , vol.19 , pp. 595-606
    • Buslepp, J.1
  • 46
    • 0031879604 scopus 로고    scopus 로고
    • Mutations in MHC class II dimer of dimers contact residues: effects on antigen presentation
    • Nydam T., et al. Mutations in MHC class II dimer of dimers contact residues: effects on antigen presentation. Int. Immunol. 10 (1998) 1237-1249
    • (1998) Int. Immunol. , vol.10 , pp. 1237-1249
    • Nydam, T.1
  • 47
    • 0035863899 scopus 로고    scopus 로고
    • Amino acid substitutions in the putative MHC class II 'dimer of dimers' interface inhibit CD4+ T cell activation
    • Lindstedt R., et al. Amino acid substitutions in the putative MHC class II 'dimer of dimers' interface inhibit CD4+ T cell activation. J. Immunol. 166 (2001) 800-808
    • (2001) J. Immunol. , vol.166 , pp. 800-808
    • Lindstedt, R.1
  • 48
    • 23144455728 scopus 로고    scopus 로고
    • T-cell receptor triggering is critically dependent on the dimensions of its peptide-MHC ligand
    • Choudhuri K., et al. T-cell receptor triggering is critically dependent on the dimensions of its peptide-MHC ligand. Nature 436 (2005) 578-582
    • (2005) Nature , vol.436 , pp. 578-582
    • Choudhuri, K.1
  • 49
    • 0029417003 scopus 로고
    • Crystal structure of the V alpha domain of a T cell antigen receptor
    • Fields B.A., et al. Crystal structure of the V alpha domain of a T cell antigen receptor. Science 270 (1995) 1821-1824
    • (1995) Science , vol.270 , pp. 1821-1824
    • Fields, B.A.1
  • 50
    • 0031048822 scopus 로고    scopus 로고
    • The efficiency of CD4 recruitment to ligand-engaged TCR controls the agonist/partial agonist properties of peptide-MHC molecule ligands
    • Madrenas J., et al. The efficiency of CD4 recruitment to ligand-engaged TCR controls the agonist/partial agonist properties of peptide-MHC molecule ligands. J. Exp. Med. 185 (1997) 219-229
    • (1997) J. Exp. Med. , vol.185 , pp. 219-229
    • Madrenas, J.1
  • 51
    • 0037474211 scopus 로고    scopus 로고
    • CD3 delta establishes a functional link between the T cell receptor and CD8
    • Doucey M.A., et al. CD3 delta establishes a functional link between the T cell receptor and CD8. J. Biol. Chem. 278 (2003) 3257-3264
    • (2003) J. Biol. Chem. , vol.278 , pp. 3257-3264
    • Doucey, M.A.1
  • 52
    • 29244457799 scopus 로고    scopus 로고
    • Mechanistic basis of pre-T cell receptor-mediated autonomous signaling critical for thymocyte development
    • Yamasaki S., et al. Mechanistic basis of pre-T cell receptor-mediated autonomous signaling critical for thymocyte development. Nat. Immunol. 7 (2006) 67-75
    • (2006) Nat. Immunol. , vol.7 , pp. 67-75
    • Yamasaki, S.1
  • 53
    • 33845790596 scopus 로고    scopus 로고
    • Molecular basis for pre-TCR-mediated autonomous signaling
    • Yamasaki S., and Saito T. Molecular basis for pre-TCR-mediated autonomous signaling. Trends Immunol. 28 (2007) 39-43
    • (2007) Trends Immunol. , vol.28 , pp. 39-43
    • Yamasaki, S.1    Saito, T.2
  • 54
    • 0031013825 scopus 로고    scopus 로고
    • T-cell antigen receptor transmembrane peptides modulate T-cell function and T cell-mediated disease
    • Manolios N., et al. T-cell antigen receptor transmembrane peptides modulate T-cell function and T cell-mediated disease. Nat. Med. 3 (1997) 84-88
    • (1997) Nat. Med. , vol.3 , pp. 84-88
    • Manolios, N.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.